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Database: UniProt
Entry: A7RVR6_NEMVE
LinkDB: A7RVR6_NEMVE
Original site: A7RVR6_NEMVE 
ID   A7RVR6_NEMVE            Unreviewed;       814 AA.
AC   A7RVR6;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Transcriptional regulator ATRX homolog {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NEMVEDRAFT_v1g94894 {ECO:0000313|EMBL:EDO44496.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO44496.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO44496.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS469544; EDO44496.1; -; Genomic_DNA.
DR   RefSeq; XP_001636559.1; XM_001636509.1.
DR   AlphaFoldDB; A7RVR6; -.
DR   STRING; 45351.A7RVR6; -.
DR   EnsemblMetazoa; EDO44496; EDO44496; NEMVEDRAFT_v1g94894.
DR   eggNOG; KOG1015; Eukaryota.
DR   HOGENOM; CLU_000315_11_3_1; -.
DR   InParanoid; A7RVR6; -.
DR   OMA; MELYTYE; -.
DR   PhylomeDB; A7RVR6; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR044574; ARIP4-like.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45797; RAD54-LIKE; 1.
DR   PANTHER; PTHR45797:SF3; RAD54-LIKE; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT   DOMAIN          128..318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          558..718
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  93376 MW;  4E98429027575F0A CRC64;
     MAKGKRKRVK EMSESEDENE EEPDTPSKSK GRRKIRKLLT DEKLGEETKK ARRLEEERRQ
     RLLERTQNLS EDMPSMDWKV DSLVLESDPE TKEPIVEVNK HIVKYLKPHQ CKGVQFMYDC
     LVESVKAYKK GEPGSGCILA HCMGLGKTLQ VVTLVHTLFN NKELEFTTAL VVAPLNTLLN
     WQVEFEKWLS HLSKPPFPIF QVYVLQEVGH NSWRRADMLT QWQRYGGIMI MGYDMYRNLS
     LCNNVRSKKV KKIFKETLVD PGPDIVICDE GHILKNDASA ISRALNAIKT RRRVVLTGTP
     LQNNLIEYHC MVSFVKPSLL GTRKEFMNTF GNPIQNGQCA DSTPSDFRIM KQRCHVLFKM
     LEGCVQRRDY SVLTPFLPAK HEYVIKVRLS EAQRKLYEHY LKTFVFPEGD VTKRGVGLFS
     DYQALMRIWT HPWCLKLEAI RRSMRMTYDD SDDSLDGFVV HTDEESESTA ESESEEDTDA
     NKGRGKSRRK DSGDEVIPEK RASGTARKTR NSLQTTRSSK PSKVEIDGED VVEVDAKPGP
     SEAEYNVELS GKLVLLLEIL ADAEAVEEKV LVFSQSLVSL DLIERALGGG EVGGDRENWC
     KGCDYFRMDG STSVQLRQRW ADIFNDPDNK TARLFLISTK AGGLGINLVA ANRVIVFDAS
     WNPSHDVQSI FRVYRFGQTK AVYVYRFLSQ GTMEERVYDR QVAKLSISER VVDKHQIERH
     FTAADLAELY KFDPDVLDET KNKEDIPSLP LPKDAILADL INRMHPQWIV KYHEHDSLLR
     NIEEEELTEE EMKIAWKAYQ DEKEAANNPA CKLR
//
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